ArticleThe Biochemical journal2016
A polybasic motif in ErbB3-binding protein 1 (EBP1) has key functions in nucleolar localization and polyphosphoinositide interaction.
Article in The Biochemical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 37 citations in OpenAlex.
- PA2G4 in health and disease: An underestimated multifunctional regulator.Journal of advanced research · 2025Review
- The nuclear phosphoinositide-p53 signalosome in the regulation of cell motility.Protein & cell · 2025Review
- Phosphoinositide signaling in the nucleus: Impacts on chromatin and transcription regulation.Biology of the cell · 2025Review
- Biomolecular condensates create phospholipid-enriched microenvironments.Nature chemical biology · 2024Article
- Non-Vesicular Lipid Transport Machinery inInternational journal of molecular sciences · 2023Review
- PI3Kα Translocation Mediates Nuclear PtdIns(3,4,5)PMolecular & cellular proteomics : MCP · 2023Article
- SAF-A/hnRNP U binds polyphosphoinositides via a lysine rich polybasic motif located in the SAP domain.microPublication biology · 2023Article
- The GpIA7 effector from the potato cyst nematode Globodera pallida targets potato EBP1 and interferes with the plant cell cycle.Journal of experimental botany · 2021Article
- Investigating the Disordered and Membrane-Active Peptide A-Cage-C Using Conformational Ensembles.Molecules (Basel, Switzerland) · 2021Article
- Systematic Screen forG3 (Bethesda, Md.) · 2020Article
- Ileal proteomic changes associated with IL-25-mediated resistance against intestinal trematode infections.Parasites & vectors · 2020Article
- Nuclear Inositides and Inositide-Dependent Signaling Pathways in Myelodysplastic Syndromes.Cells · 2020Review
- MetAP-like Ebp1 occupies the human ribosomal tunnel exit and recruits flexible rRNA expansion segments.Nature communications · 2020Article
- The nuclear phosphoinositide response to stress.Cell cycle (Georgetown, Tex.) · 2020Review
- ErbB-3 BINDING PROTEIN 1 Regulates Translation and Counteracts RETINOBLASTOMA RELATED to Maintain the Root Meristem.Plant physiology · 2020Article
- Review
- Class I Phosphoinositide 3-KinaseInternational journal of molecular sciences · 2018Review
- Non-vesicular Lipid Transport Machinery inFrontiers in cellular and infection microbiology · 2018Review
- Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Polyphosphoinositides (PPIns) are present in the nucleus where they participate in crucial nuclear processes, such as chromatin remodelling, transcription and mRNA processing. In a previous interactomics study, aimed to gain further insight into nuclear PPIns functions, we identified ErbB3 binding protein 1 (EBP1) as a potential nuclear PPIn-binding protein in a lipid pull-down screen. EBP1 is a ubiquitous and conserved protein, located in both the cytoplasm and nucleolus, and associated with cell proliferation and survival. In the present study, we show that EBP1 binds directly to several PPIns via two distinct PPIn-binding sites consisting of clusters of lysine residues and positioned at the N- and C-termini of the protein. Using interaction mutants, we show that the C-terminal PPIn-binding motif contributes the most to the localization of EBP1 in the nucleolus. Importantly, a K372N point mutation, located within the C-terminal motif and found in endometrial tumours, is sufficient to alter the nucleolar targeting of EBP1. Our study reveals also the presence of the class I phosphoinositide 3-kinase (PI3K) catalytic subunit p110β and its product PtdIns(3,4,5)P3 together with EBP1 in the nucleolus. Using NMR, we further demonstrate an association between EBP1 and PtdIns(3,4,5)P3 via both electrostatic and hydrophobic interactions. Taken together, these results show that EBP1 interacts directly with PPIns and associate with PtdIns(3,4,5)P3 in the nucleolus. The presence of p110β and PtdIns(3,4,5)P3 in the nucleolus indicates their potential role in regulating nucleolar processes, at least via EBP1.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.